Research workbench
NMR structure of the arid domain from the histone H3K4 demethylase RBP2
Analyse NMR structure of the arid domain from the histone H3K4 demethylase RBP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JXJ
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone demethylase JARID1A
- EC
- 1.14.11.-
- UniProt
- P29375
- Pockets
- 1 · best druggability 0.59
Structure
solution nmr · 1 distinct chain · 65% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone demethylase JARID1A (EC 1.14.11.-) | protein | 96 | 65% helix, 4% strand | P29375 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.59 | 0.90 | 14 | empty |
Compared structures
- 2JXJ · NMR structure of the ARID domain from the histone H3K4 demethylase RBP2 · the same entry in another collection · chain A against A, TM-score 1.00
- P29375 · AlphaFold monomer V2.0 prediction for lysine-specific demethylase 5A (P29375) · a predicted model of the same protein · chain A against A, TM-score 0.87
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29375
- Elsewhere: RCSB PDB 2JXJ · PDBe 2JXJ · UniProt P29375
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